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일반 설명
Concanavalin A is isolated from the from Canavalia ensiformis (Jack bean). It is a mitogenic lectin with a dome-like structures and is a tetrameric protein.
애플리케이션
Concanavalin A from Canavalia ensiformis (Jack bean) has been used:
- in the colabelling of fischer rat thyroid (FRT) epithelia(104)
- to induce autoimmune hepatitis in Cre-conditional atg7 knockout mice(105)
- to detect glycoproteins containing α-D-mannose, α-D-glucose when used with avidin or streptavidin detection system(106)
생화학적/생리학적 작용
Con A is not blood group specific but has an affinity for terminal α-D-mannosyl and α-D-glucosyl residues. Ca2+ and Mn2+ ions are required for activity. Con A dissociates into dimers at pH 5.6 or below. Between pH 5.8 and pH 7.0, Con A exists as a tetramer; above pH 7.0 higher aggregates are formed. Con A exhibits mitogenic activity which is dependent on its degree of aggregation. Succinylation results in an active dimeric form which remains a dimer above pH 5.6.
Concanavalin A (Con A) bound to glycoenzyme has wide applications and can be dissociated in the presence of high sugar levels. Con A induces hepatic inflammation. It stimulates macrophages and promotes cytokine production. Con A also exhibits anti-hepatoma effect and could be used effectively as a vaccine for treating cancer.
포장
Package size based on protein content
물리적 형태
Contains sodium citrate
분석 메모
Where reported, agglutination activity is expressed in μg/ml and is determined from serial dilutions in phosphate buffered saline, pH 6.8, containing Ca2+ and Mn2+ of a 1 mg per mL solution. This activity is the lowest concentration to agglutinate a 2% suspension of human erythrocytes after 1 hr incubation at 25 °C.
이미 열람한 고객
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